Target Details ABCC8

SUR1 is a 1581 amino acid protein with an ATP binding domain with two nucleotide binding folds (NBFs) and binding sites for sulfonylureas, like glibenclamide, and for channel openers. SUR contains three hydrophobic domains, TM(0), TM(1), and TM(2), with nucleotide binding folds following TM(1) and TM(2). The protein is glycosylated at position 10 on Asn. The SUR1 gene is expressed in at least 4 multiple splice variants ere are multiple splice variants, these splice variants originate from the splicing of the coding region of NFB and lack of axon 17 (SUR1 Delta 17), axon 19 (SUR1 Delta 19) and both (SUR1 Delta 17/19) and the fourth is a COOH terminal fragment formed by Exxon 31-39 containing the last 2 TMD and the COOH terminal (SUR1C). The various splice variants of SUR1 are expressed in various tissues with strong expression of SUR1C in cardiomyocytes. Only SUR1 and SUR1Delta 17 exhibit high affinity binding sites for sulfonylurea and other pharmacological agents. Several point mutations in the NFB region of SUR1 are also described in NIDDM. A total of five amino acid substitutions and 17 silent mutations were noted by examining all 39 axons of this gene in NIDDM patients form Japan. Two rare novel mutations, D811N in axon 20 and R835C in axon 21, were identified in the first nucleotide binding fold (NBF), a functionally important region of SUR1, in one patient each, both heterozygotes.Synonyms: ATP-binding cassette transporter sub-family C member 8, HRINS, SUR, SUR1, Sulfonylurea receptor 1